一种用于免疫球蛋白及其他蛋白质微量碘化的酶法。
An enzymic method for the trace iodination of immunoglobulins and other proteins.
作者信息
Marchalonis J J
出版信息
Biochem J. 1969 Jun;113(2):299-305. doi: 10.1042/bj1130299.
Abstract
- A method is described for the trace iodination of immunoglobulins and other serum proteins by a system consisting of lactoperoxidase, hydrogen peroxide and iodide. 2. gammaG immunoglobulin that had been labelled to a specific radioactivity of 5muc/mug. by use of carrier-free [(125)I]iodide gave no evidence of denaturation when analysed by electrophoresis and density-gradient ultracentrifugation. 3. Tryptic hydrolysis and peptide ;mapping' of a completely characterized peptide radioiodinated by this method showed that the [(125)I]iodide was bound to tyrosyl residues. 4. Proteins differ in their susceptibility to iodination by this method. Human gammaG immunoglobulin, for example, is iodinated more than ten times as readily as is human alpha(2)-macroglobulin under the same conditions. 5. Lactoperoxidase catalyses the iodination of proteins much more readily than does horseradish peroxidase.
摘要
- 描述了一种通过由乳过氧化物酶、过氧化氢和碘化物组成的系统对免疫球蛋白和其他血清蛋白进行微量碘化的方法。2. 使用无载体[(125)I]碘化物标记至比放射性为5μCi/μg的γG免疫球蛋白，经电泳和密度梯度超速离心分析未显示变性迹象。3. 对用该方法进行放射性碘化的一个完全表征的肽进行胰蛋白酶水解和肽“图谱分析”表明，[(125)I]碘化物与酪氨酸残基结合。4. 蛋白质对该方法碘化的敏感性不同。例如，在相同条件下，人γG免疫球蛋白的碘化速度比人α(2)-巨球蛋白快十多倍。5. 乳过氧化物酶比辣根过氧化物酶更容易催化蛋白质的碘化。
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